Boswell A P, Moore G R, Williams R J, Wallace C J, Boon P J, Nivard R J, Tesser G I
Biochem J. 1981 Feb 1;193(2):493-502. doi: 10.1042/bj1930493.
1H n.m.r. spectra were recorded in both oxidation states for the following species: tuna cytochrome c, tuna [carboxymethylmethionine-65]cytochrome c, horse cytochrome c and horse [homoserine-65]cytochrome c. The experiments give the assignments of the singlet methyl resonances of methionine-65 and the N-terminal acetyl group. The modification at methionine-65 is shown to cause an extremely small structural perturbation to one part of the molecule close to the site of modification.
记录了以下物种在两种氧化态下的1H核磁共振谱:金枪鱼细胞色素c、金枪鱼[羧甲基甲硫氨酸-65]细胞色素c、马细胞色素c和马[高丝氨酸-65]细胞色素c。实验给出了甲硫氨酸-65的单峰甲基共振和N端乙酰基的归属。结果表明,甲硫氨酸-65处的修饰对分子中靠近修饰位点的一部分结构产生了极小的扰动。